1p9l

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[[Image:1p9l.gif|left|200px]]
[[Image:1p9l.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1p9l |SIZE=350|CAPTION= <scene name='initialview01'>1p9l</scene>, resolution 2.3&Aring;
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The line below this paragraph, containing "STRUCTURE_1p9l", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PDC:PYRIDINE-2,6-DICARBOXYLIC+ACID'>PDC</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrodipicolinate_reductase Dihydrodipicolinate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.26 1.3.1.26] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= dapB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam05173 DapB_C], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam01113 DapB_N]</span>
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{{STRUCTURE_1p9l| PDB=1p9l | SCENE= }}
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|RELATEDENTRY=[[1arz|1ARZ]], [[1dih|1DIH]], [[1c3v|1C3V]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9l OCA], [http://www.ebi.ac.uk/pdbsum/1p9l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p9l RCSB]</span>
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}}
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'''Structure of M. tuberculosis dihydrodipicolinate reductase in complex with NADH and 2,6 PDC'''
'''Structure of M. tuberculosis dihydrodipicolinate reductase in complex with NADH and 2,6 PDC'''
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
[[Category: TBSGC, TB Structural Genomics Consortium.]]
[[Category: Zheng, R.]]
[[Category: Zheng, R.]]
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[[Category: lysine biosynthesis]]
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[[Category: Lysine biosynthesis]]
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[[Category: nadh binding specificity]]
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[[Category: Nadh binding specificity]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: protein structure initiative]]
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[[Category: Protein structure initiative]]
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[[Category: psi]]
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[[Category: Psi]]
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[[Category: reductase]]
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[[Category: Reductase]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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[[Category: tb structural genomics consortium]]
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[[Category: Tb structural genomics consortium]]
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[[Category: tbsgc]]
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[[Category: Tbsgc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:51:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:56:48 2008''
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Revision as of 01:51, 3 May 2008

Image:1p9l.gif

Template:STRUCTURE 1p9l

Structure of M. tuberculosis dihydrodipicolinate reductase in complex with NADH and 2,6 PDC


Overview

Dihydrodipicolinate reductase (DHPR) catalyzes the reduced pyridine nucleotide-dependent reduction of the alpha,beta-unsaturated cyclic imine, dihydrodipicolinate, to generate tetrahydrodipicolinate. This enzyme catalyzes the second step in the bacterial biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine. The Mycobacterium tuberculosis dapB-encoded DHPR has been cloned, expressed, purified, and crystallized in two ternary complexes with NADH or NADPH and the inhibitor 2,6-pyridinedicarboxylate (2,6-PDC). The structures have been solved using molecular replacement strategies, and the DHPR-NADH-2,6-PDC and DHPR-NADPH-2,6-PDC complexes have been refined against data to 2.3 and 2.5 A, respectively. The M. tuberculosis DHPR is a tetramer of identical subunits, with each subunit composed of two domains connected by two flexible hinge regions. The N-terminal domain binds pyridine nucleotide, while the C-terminal domain is involved in both tetramer formation and substrate/inhibitor binding. The M. tuberculosis DHPR uses NADH and NADPH with nearly equal efficiency based on V/K values. To probe the nature of this substrate specificity, we have generated two mutants, K9A and K11A, residues that are close to the 2'-phosphate of NADPH. These two mutants exhibit decreased specificity for NADPH by factors of 6- and 30-fold, respectively, but the K11A mutant exhibits 270% of WT activity using NADH. The highly conserved structure of the nucleotide fold may permit other enzyme's nucleotide specificity to be altered using similar mutagenic strategies.

About this Structure

1P9L is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2,6-PDC and -NADPH-2,6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity., Cirilli M, Zheng R, Scapin G, Blanchard JS, Biochemistry. 2003 Sep 16;42(36):10644-50. PMID:12962488 Page seeded by OCA on Sat May 3 04:51:14 2008

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